Temperature, organic solvent and pH stabilization of the neutral protease from Salinovibrio proteolyticus: significance of the structural calcium.

Abstract:

:In order to clarify the impact of Ca-binding sites (Ca1 and 2) on the conformational stability of neutral proteases (NPs), we have analyzed the thermal, pH and organic solvent stability of a NP variant, V189P/A195E/G203D/A268E (Q-mutant), from Salinovibrio proteolyticus. This mutant has shown to bind calcium more tightly than the wild-type (WT) at Ca1 and to possess Ca2. Q-mutant was resisted against autolysis, thermoinactivation and pH denaturation in a Ca-dependent manner and exhibited better activity in organic solvents compared to the WT enzyme. These results imply that Ca1 and Ca2 are important for the conformational stability of NPs.

journal_name

BMB Rep

journal_title

BMB reports

authors

Asghari SM,Khajeh K,Dalfard AB,Pazhang M,Karbalaei-Heidari HR

doi

10.5483/BMBRep.2011.44.10.665

subject

Has Abstract

pub_date

2011-10-01 00:00:00

pages

665-8

issue

10

eissn

1976-6696

issn

1976-670X

journal_volume

44

pub_type

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